ADI1

The human ADI1 gene encodes the enzyme 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase.[5][6][7]

ADI1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesADI1, APL1, ARD, Fe-ARD, MTCBP1, Ni-ARD, SIPL, mtnD, HMFT1638, acireductone dioxygenase 1
External IDsOMIM: 613400 MGI: 2144929 HomoloGene: 75081 GeneCards: ADI1
Gene location (Human)
Chr.Chromosome 2 (human)[1]
Band2p25.3Start3,497,366 bp[1]
End3,519,531 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

55256

104923

Ensembl

ENSG00000280830
ENSG00000182551

ENSMUSG00000020629

UniProt

Q9BV57

Q99JT9

RefSeq (mRNA)

NM_001306077
NM_018269

NM_134052

RefSeq (protein)

NP_001293006
NP_060739

NP_598813

Location (UCSC)Chr 2: 3.5 – 3.52 MbChr 12: 28.68 – 28.68 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

The enzyme belongs to the aci-reductone dioxygenase family of metal-binding enzymes, which are involved in methionine salvage. This enzyme may regulate mRNA processing in the nucleus, and may carry out different functions depending on its localization.

Clinical significance

Diseases associated with ADI1 include Klebsiella, and refsum disease.

ADI1 is capable for supporting hepatitis C virus replication in an otherwise non-permissive cell line.[8] Mouse hepatoma cells coexpressing human CD81 and ADI1/Sip-L supported HCV infection and replication.[9] Human ADI1//Sip-L over-expression in 293 cells enhances cell entry but not replication of HCV.[10][11]

References

  1. ENSG00000182551 GRCh38: Ensembl release 89: ENSG00000280830, ENSG00000182551 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000020629 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Uekita T, Gotoh I, Kinoshita T, Itoh Y, Sato H, Shiomi T, Okada Y, Seiki M (Mar 2004). "Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein-1 is a new member of the Cupin superfamily. A possible multifunctional protein acting as an invasion suppressor down-regulated in tumors". J Biol Chem. 279 (13): 12734–43. doi:10.1074/jbc.M309957200. PMID 14718544.
  6. Hirano W, Gotoh I, Uekita T, Seiki M (Jun 2005). "Membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-1 (MTCBP-1) acts as an eukaryotic aci-reductone dioxygenase (ARD) in the methionine salvage pathway". Genes Cells. 10 (6): 565–74. doi:10.1111/j.1365-2443.2005.00859.x. PMID 15938715. S2CID 25563839.
  7. "Entrez Gene: ADI1 acireductone dioxygenase 1".
  8. Yeh CT, Lai HY, Chen TC, Chu CM, Liaw YF (2001). "Identification of a hepatic factor capable of supporting hepatitis C virus replication in a nonpermissive cell line". J. Virol. 75 (22): 11017–24. doi:10.1128/JVI.75.22.11017-11024.2001. PMC 114682. PMID 11602742.
  9. Yeh CT, Lai HY, Yeh YJ, Cheng JC (2008). "Hepatitis C virus infection in mouse hepatoma cells co-expressing human CD81 and Sip-L". Biochem Biophys Res Commun. 372 (1): 157–61. doi:10.1016/j.bbrc.2008.05.018. PMID 18474223.
  10. Cheng JC, Yeh YJ, Pai LM, Chang ML, Yeh CT (2009). "293 cells over-expressing human ADI1 and CD81 are permissive for serum-derived hepatitis C virus infection". J. Med. Virol. 81 (9): 1560–8. doi:10.1002/jmv.21495. PMID 19626614. S2CID 27972307.
  11. Hwang DR, Lai HY, Chang ML, Hsu JT, Yeh CT (2005). "Emergence of mutation clusters in the HCV genome during sequential viral passages in Sip-L expressing cells". J Virol Methods. 129 (2): 170–7. doi:10.1016/j.jviromet.2005.05.026. PMID 16005986.

Further reading


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